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Database: UniProt
Entry: A0A445JSD7_GLYSO
LinkDB: A0A445JSD7_GLYSO
Original site: A0A445JSD7_GLYSO 
ID   A0A445JSD7_GLYSO        Unreviewed;      1103 AA.
AC   A0A445JSD7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Tyrosine-sulfated glycopeptide receptor 1 {ECO:0000313|EMBL:RZC01404.1};
GN   ORFNames=D0Y65_016907 {ECO:0000313|EMBL:RZC01404.1};
OS   Glycine soja (Wild soybean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3848 {ECO:0000313|EMBL:RZC01404.1, ECO:0000313|Proteomes:UP000289340};
RN   [1] {ECO:0000313|EMBL:RZC01404.1, ECO:0000313|Proteomes:UP000289340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC   TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZC01404.1};
RA   Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT   "A high-quality reference genome of wild soybean provides a powerful tool
RT   to mine soybean genomes.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|ARBA:ARBA00008684}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RZC01404.1}.
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DR   EMBL; QZWG01000007; RZC01404.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445JSD7; -.
DR   OrthoDB; 831390at2759; -.
DR   Proteomes; UP000289340; Chromosome 7.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR45974:SF95; OS02G0153700 PROTEIN; 1.
DR   PANTHER; PTHR45974; RECEPTOR-LIKE PROTEIN 55; 1.
DR   Pfam; PF00560; LRR_1; 8.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52058; L domain-like; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51450; LRR; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Receptor {ECO:0000313|EMBL:RZC01404.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289340};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        25..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        733..757
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          820..1091
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         849
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1103 AA;  120829 MW;  CB36E00B5C7719EA CRC64;
     MTNHHLKHSI LSSVFLMPSP SSSSFAYSLY MVSKLMVTII VPLFLLSLFV VQVSSCNQID
     KLSLLAFSGN ISTSPPYPSL NWSDSLDCCS WEGITCDGDL RVTHLLLPSR GLTGFISPSL
     TNLSSLSQLN LSHNRLSGTL QHHFFSLLNH LLVLDLSYNR LSGELPPFVG DISGKNSSGG
     VIQELDLSSN LFNGTLPNSL LEHLAAAAAG GSFVSLNVSN NSLTGHIPTS LFCVNDHNSS
     SLRFLDYSSN EFDGAIQPGL GACSKLEKFK AGFNFLSGPI PSDLFDAVSL TEISLPLNRL
     TGTIADGIVG LTNLTVLELY SNHFTGSIPH DIGELSKLER LLLHVNNLTG TMPPSLINCV
     NLVVLNLRVN LLEGNLSAFN FSRFLGLTTL DLGNNHFTGV LPPTLYACKS LSAVRLASNK
     LEGEISPKIL ELESLSFLSI STNKLRNVTG ALRILRGLKN LSTLMLSMNF FNEMIPQDVN
     IIEPDGFQKL QVLGFGGCNF TGQIPGWLVK LKKLEALDLS FNQISGPIPL WLGTLPQLFY
     MDLSVNLLTG VFPVELTELP ALASQQANDK VERTYFELPV FANANNVSLL QYNQLSGLPP
     AIYLGSNHLN GSIPIEIGKL KVLHQLDLKK NNFSGNIPVQ FSNLTNLEKL DLSGNQLSGE
     IPDSLRRLHF LSFFSVAFNN LQGQIPTGGQ FDTFSNSSFE GNVQLCGLVI QRSCPSQQNT
     NTTAASRSSN KKVLLVLIIG VSFGFAFLIG VLTLWILSKR RVNPGGVSDK IEMESISAYS
     NSGVHPEVDK EASLVVLFPN KNNETKDLTI FEILKSTENF SQANIIGCGG FGLVYKATLP
     NGTTLAIKKL SGDLGLMERE FKAEVEALST AQHENLVALQ GYGVHDGFRL LMYNYMENGS
     LDYWLHEKPD GASQLDWPTR LKIAQGASCG LAYLHQICEP HIVHRDIKSS NILLNEKFEA
     HVADFGLSRL ILPYHTHVTT ELVGTLGYIP PEYGQAWVAT LRGDVYSFGV VMLELLTGRR
     PVDVCKPKMS RELVSWVQQM RIEGKQDQVF DPLLRGKGFE GQMLKVLDVA SVCVSHNPFK
     RPSIREVVEW LKNVGSDNQP TQK
//
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